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Results: 1 to 3 of 3

Publication Record


Laminin-111 peptide C16 regulates invadopodia activity of malignant cells through β1 integrin, Src and ERK 1/2.
Siqueira AS, Pinto MP, Cruz MC, Smuczek B, Cruz KS, Barbuto JA, Hoshino D, Weaver AM, Freitas VM, Jaeger RG
(2016) Oncotarget 7: 47904-47917
MeSH Terms: Carcinoma, Squamous Cell, Cell Line, Tumor, Fibrosarcoma, Head and Neck Neoplasms, Humans, Integrin beta1, Laminin, MAP Kinase Signaling System, Mouth Neoplasms, Peptide Fragments, Podosomes, Squamous Cell Carcinoma of Head and Neck, Transfection, src-Family Kinases
Show Abstract · Added April 26, 2017
Laminin peptides influence tumor behavior. In this study, we addressed whether laminin peptide C16 (KAFDITYVRLKF, γ1 chain) would increase invadopodia activity of cells from squamous cell carcinoma (CAL27) and fibrosarcoma (HT1080). We found that C16 stimulates invadopodia activity over time in both cell lines. Rhodamine-conjugated C16 decorates the edge of cells, suggesting a possible binding to membrane receptors. Flow cytometry showed that C16 increases activated β1 integrin, and β1 integrin miRNA-mediated depletion diminishes C16-induced invadopodia activity in both cell lines. C16 stimulates Src and ERK 1/2 phosphorylation, and ERK 1/2 inhibition decreases peptide-induced invadopodia activity. C16 also increases cortactin phosphorylation in both cells lines. Based on our findings, we propose that C16 regulates invadopodia activity over time of squamous carcinoma and fibrosarcoma cells, probably through β1 integrin, Src and ERK 1/2 signaling pathways.
0 Communities
1 Members
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14 MeSH Terms
Regulation of invadopodia by mechanical signaling.
Parekh A, Weaver AM
(2016) Exp Cell Res 343: 89-95
MeSH Terms: Extracellular Matrix, Humans, Mechanotransduction, Cellular, Models, Biological, Podosomes, Tumor Microenvironment
Show Abstract · Added February 15, 2016
Mechanical rigidity in the tumor microenvironment is associated with a high risk of tumor formation and aggressiveness. Adhesion-based signaling driven by a rigid microenvironment is thought to facilitate invasion and migration of cancer cells away from primary tumors. Proteolytic degradation of extracellular matrix (ECM) is a key component of this process and is mediated by subcellular actin-rich structures known as invadopodia. Both ECM rigidity and cellular traction stresses promote invadopodia formation and activity, suggesting a role for these structures in mechanosensing. The presence and activity of mechanosensitive adhesive and signaling components at invadopodia further indicates the potential for these structures to utilize myosin-dependent forces to probe and remodel their ECM environments. Here, we provide a brief review of the role of adhesion-based mechanical signaling in controlling invadopodia and invasive cancer behavior.
Copyright © 2015 Elsevier Inc. All rights reserved.
2 Communities
2 Members
0 Resources
6 MeSH Terms
Polyacrylamide gels for invadopodia and traction force assays on cancer cells.
Jerrell RJ, Parekh A
(2015) J Vis Exp : 52343
MeSH Terms: Acrylic Resins, Actins, Biomechanical Phenomena, Cell Movement, Extracellular Matrix, Humans, Neoplasms, Podosomes, Proteolysis, Tumor Microenvironment
Show Abstract · Added January 20, 2015
Rigid tumor tissues have been strongly implicated in regulating cancer cell migration and invasion. Invasive migration through cross-linked tissues is facilitated by actin-rich protrusions called invadopodia that proteolytically degrade the extracellular matrix (ECM). Invadopodia activity has been shown to be dependent on ECM rigidity and cancer cell contractile forces suggesting that rigidity signals can regulate these subcellular structures through actomyosin contractility. Invasive and contractile properties of cancer cells can be correlated in vitro using invadopodia and traction force assays based on polyacrylamide gels (PAAs) of different rigidities. Invasive and contractile properties of cancer cells can be correlated in vitro using invadopodia and traction force assays based on polyacrylamide gels (PAAs) of different rigidities. While some variations between the two assays exist, the protocol presented here provides a method for creating PAAs that can be used in both assays and are easily adaptable to the user's specific biological and technical needs.
1 Communities
1 Members
0 Resources
10 MeSH Terms